Extended Data Fig. 2: Structural comparison of different receptor-arrestin interfaces. | Nature Chemical Biology

Extended Data Fig. 2: Structural comparison of different receptor-arrestin interfaces.

From: Molecular basis of β-arrestin coupling to the metabotropic glutamate receptor mGlu3

Extended Data Fig. 2: Structural comparison of different receptor-arrestin interfaces.

(a) Superimposition of βarr1 (blue) from the mGlu3-βarr1 complex with arrestins (yellow) from various receptor-arrestin complexes. The TMD of mGlu3, serving as a guide for membrane positioning, is colored grey. Arrows indicate the position of the FLR of arrestins. (b) Superimposition of the TMD from the mGlu3-βarr1 complex with TMDs from other receptor-arrestin complexes. βarr1 from the mGlu3-βarr1 complex and arrestins from other receptor-arrestin complexes are colored blue and yellow, respectively. Dash lines (cyan and orange) represent the approximate long-axis positions of the arrestin molecules. The two arrestin molecules are not positioned on the same two-dimensional planes, so the angles between two dash lines on the paper plane are estimated and labeled. The following PDB codes were used: V2R-βarr1 (7R0C); Rhodopsin-Varr (5W0P); 5-HT2BR-βarr1 (7SRS); GCGR-βarr1 (8JRV); β1AR-βarr1 (6TKO); M2R-βarr1 (6U1N); CB1-βarr1 (8WU1); NTSR1-βarr1-1 (6UP7); NTSR1-βarr1-2 (6PWC).

Back to article page